ID A0A074W2D2_9PEZI Unreviewed; 829 AA.
AC A0A074W2D2;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Putative N,N-dimethylglycine oxidase {ECO:0000313|EMBL:KEQ65684.1};
GN ORFNames=M437DRAFT_41348 {ECO:0000313|EMBL:KEQ65684.1};
OS Aureobasidium melanogenum CBS 110374.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043003 {ECO:0000313|EMBL:KEQ65684.1, ECO:0000313|Proteomes:UP000030672};
RN [1] {ECO:0000313|EMBL:KEQ65684.1, ECO:0000313|Proteomes:UP000030672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110374 {ECO:0000313|EMBL:KEQ65684.1,
RC ECO:0000313|Proteomes:UP000030672};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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DR EMBL; KL584826; KEQ65684.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074W2D2; -.
DR STRING; 1043003.A0A074W2D2; -.
DR HOGENOM; CLU_007884_11_2_1; -.
DR OrthoDB; 1815533at2759; -.
DR Proteomes; UP000030672; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.40.30.110; Aminomethyltransferase beta-barrel domains; 1.
DR Gene3D; 3.30.70.1400; Aminomethyltransferase beta-barrel domains; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR032503; FAO_M.
DR InterPro; IPR028896; GCST/YgfZ/DmdA.
DR InterPro; IPR013977; GCV_T_C.
DR InterPro; IPR006222; GCV_T_N.
DR InterPro; IPR029043; GcvT/YgfZ_C.
DR InterPro; IPR027266; TrmE/GcvT_dom1.
DR PANTHER; PTHR43757; AMINOMETHYLTRANSFERASE; 1.
DR PANTHER; PTHR43757:SF2; AMINOMETHYLTRANSFERASE, MITOCHONDRIAL; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF16350; FAO_M; 1.
DR Pfam; PF01571; GCV_T; 1.
DR Pfam; PF08669; GCV_T_C; 1.
DR SUPFAM; SSF101790; Aminomethyltransferase beta-barrel domain; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF103025; Folate-binding domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000030672}.
FT DOMAIN 5..372
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 376..431
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 433..719
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 743..821
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 829 AA; 91239 MW; 8B59827BB12868BC CRC64;
MYSPRVVIIG AGIVGTNVAD ELVARGWTNI TVVDQGPLDM PGGSTSHAPG LVFQTNVCKT
MTLFAKYTVE KLKALEEDGE NCFNQVGGLE IATDEARLAE IKRKHGYAQS WGIEAHLISP
EECMEKYPLL NKEQVLGGLH IPTDGLAKAA RAVQLLINRT RKAGVQYIDK TPVTGIAKAD
GHVTGVETPN GTIPADIVVS CAGFWGVEIG AMIGLPIPLL PLAHQYVKTT SVPALAKRNN
PEGGASLPIL RYQDQDLYYR EHGDQYGIGY YGHKPMPVVA ASLGVTPEKV DHKNMPSRLE
FTREDFEPAW ELSKKFLPCM DEVEIEDGFN GIFSFTPDGG SLVGHAPNLE GFYVAEAVWV
THSAGIARAV AEVLTTGKSQ IDLGAVELNR FEEVQLTSSY VKETSMQNFV EIYDIMHPLQ
PRESPRNLRV SPFHARQKEL GAYFLEGGAW ERPYWFEANE KLVKDLPEEW KPKDRDAWSS
RYYSPIAAAE AWKTRTAAAM YDMTPLRRLE VYGPGAVDLL QRVSTGDVGK KPGAVTYTLW
LDDRGGIKSD VTVARIEDQL FQVGCNGPVD LVFLNKEAAK QMQEDPTKWC TIRDITSGTC
CIGLWGPKVR EIISKVSQDD FSSTAKGLRY FRTKRAYIAG IPVTIMRLSY VGELGWEIYT
TADRGQALWD ALWEAGQEQG IIAAGRTAFN ALRLEKGYRS WGSDMNTEHD PYEAGVGFAV
KAGKVGYYGQ AALEGRSVET AKKRLRCLVV DDGSSVVLGR EPVFVGGKPS GYVTSAAFAY
TIGKPIAYAW LPSSINEDDK VEIEYFGKRI EATVTAEPLF DPSMSRLRG
//